nonidet-p40 Roche Search Results


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  • 99
    Millipore lacz wash buffer
    Lacz Wash Buffer, supplied by Millipore, used in various techniques. Bioz Stars score: 99/100, based on 14 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Roche nonidet p40
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Nonidet P40, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 4080 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Roche nonidet p40 substitute
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Nonidet P40 Substitute, supplied by Roche, used in various techniques. Bioz Stars score: 93/100, based on 36 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Roche detergent nonidet p40
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Detergent Nonidet P40, supplied by Roche, used in various techniques. Bioz Stars score: 86/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Roche nonidet p40 np40
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Nonidet P40 Np40, supplied by Roche, used in various techniques. Bioz Stars score: 93/100, based on 15 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    91
    Roche nonidet p40 buffer
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Nonidet P40 Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 91/100, based on 26 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Roche reagents nonidet p40
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Reagents Nonidet P40, supplied by Roche, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Roche nonidet p40 plus protease inhibitor cocktails
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Nonidet P40 Plus Protease Inhibitor Cocktails, supplied by Roche, used in various techniques. Bioz Stars score: 86/100, based on 4 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    85
    Roche detergent nonidet p40 np40
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Detergent Nonidet P40 Np40, supplied by Roche, used in various techniques. Bioz Stars score: 85/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    93
    Roche nonidet p40 lysis buffer
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Nonidet P40 Lysis Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 93/100, based on 83 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    92
    Roche nonidet p40 np 40
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Nonidet P40 Np 40, supplied by Roche, used in various techniques. Bioz Stars score: 92/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    86
    Roche enzyme compatible solvent system isopropanol nonidat p40
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Enzyme Compatible Solvent System Isopropanol Nonidat P40, supplied by Roche, used in various techniques. Bioz Stars score: 86/100, based on 8 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    np40  (Roche)
    99
    Roche np40
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Np40, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 7393 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Roche np40 lysis buffer
    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, <t>Nonidet</t> <t>P40;</t> Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.
    Np40 Lysis Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 96/100, based on 1202 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Roche ripa buffer
    Automethylation of SUV39H2 is validated in vivo A. Determination of the titer and specificity of the anti-K392 dimethylated SUV39H2 (Sigma-Aldrich) antibody analyzed by enzyme-linked immunosorbent assay (ELISA). A constant amount of K392 methyl peptide or unmethyl peptide has been coated into the wells of the ELISA, and tested with different dilutions of the antibody. B. His-tagged SUV39H2 recombinant proteins were incubated with or without the cofactor SAM at 30°C for 2 hours. Automethylated SUV39H2 protein was blotted with the anti-SUV39H2 K392me2 antibody, and amounts of loading SUV39H2 recombinant proteins were measured by staining with Coomassie Brilliant Blue. C. In vivo methyltransferase experiment was conducted in <t>293T</t> cells overexpressing FLAG control empty vector (FLAG-Mock), FLAG-tagged SUV39H2 wild-type (FLAG-SUV39H2-WT), FLAG-tagged SUV39H2 K392A mutant (FLAG-SUV39H2-K392A) or FLAG-tagged SUV39H2 K392R mutant (FLAG-SUV39H2-K293R). Cells were lysed with <t>RIPA</t> buffer 48 hours after transfection, and samples were immunoblotted with anti-FLAG and anti-SUV39H2 K392me2 antibodies.
    Ripa Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 37592 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    96
    Roche immunoprecipitation buffer
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Immunoprecipitation Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 96/100, based on 1416 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Roche lysis buffer
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Lysis Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 110386 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Roche tris hcl buffer
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Tris Hcl Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 1635 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    99
    Roche np 40 lysis buffer
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Np 40 Lysis Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 3675 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Np40 Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 98/100, based on 908 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche ripa lysis buffer
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Ripa Lysis Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 8787 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche buffer
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 98/100, based on 7370 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche wash buffer
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Wash Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 1832 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche buffer a
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Buffer A, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 11917 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche radioimmunoprecipitation assay ripa buffer
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Radioimmunoprecipitation Assay Ripa Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 2715 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche post transfection
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Post Transfection, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 4511 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche nonidet lysis buffer
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Nonidet Lysis Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 86/100, based on 13 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
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    Roche radioimmunoprecipitation assay buffer
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Radioimmunoprecipitation Assay Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 4153 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Radioimmuno Precipitation Assay Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 92/100, based on 68 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Roche radioimmunoprecipitation assay lysis buffer
    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Radioimmunoprecipitation Assay Lysis Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 99/100, based on 850 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 <t>immunoprecipitation</t> (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P
    Immunoprecipitation Lysis Buffer, supplied by Roche, used in various techniques. Bioz Stars score: 93/100, based on 222 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Image Search Results


    Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, Nonidet P40; Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.

    Journal: Biology of the cell

    Article Title: Lys-110 is essential for targeting PCNA to replication and repair foci, and the K110A mutant activates apoptosis

    doi: 10.1042/BC20070158

    Figure Lengend Snippet: Substitution of Lys-110 with an alanine residue results in the accumulation of the mutant PCNA in the heterochromatin region ( A ) The cell fractionation protocol. CHO cells transfected with WT or mutant constructs were fractionated at 12 h post-transfection. MNase, micrococcal nuclease; NP-40, Nonidet P40; Sup, supernatant. ( B ) Fractionated samples were analysed by SDS/PAGE and Western blotting with anti-GFP, -PCNA, -(histone H1) or -HP1α antibodies as indicated. The striking differences in chromatin localization of PCNA(K110A) and endogenous PCNA are shown with * and arrowheads. ( C ) DNA purified from each fraction was separated by agarose gel electrophoresis (2% gel). Di, di-nucleosome; M, DNA size makers; Mono, mononucleosome.

    Article Snippet: Briefly, nuclei were lysed in lysis buffer [15 mM Tris/HCl (pH 7.4), 60 mM KCl, 15 mM MgCl2 , 15 mM NaCl, 1mM CaCl2 , 1 mM PMSF, 0.6% Nonidet P40 and 1×protease inhibitor cocktail (Roche)].

    Techniques: Mutagenesis, Cell Fractionation, Transfection, Construct, SDS Page, Western Blot, Purification, Agarose Gel Electrophoresis

    Analyses of HA/CD44-mediated HOXD10 and RhoGTPase expression in MDA-MB-231 cells.  Detection of HA/CD44-induced HOXD10 and RhoGTPase (RhoA/RhoC) expression in MDA-MB-231 cells was performed by solubilizing cells with 1% Nonidet P-40 (Nonidet P-40) buffer

    Journal: The Journal of Biological Chemistry

    Article Title: Hyaluronan-CD44 Interaction Promotes c-Src-mediated Twist Signaling, MicroRNA-10b Expression, and RhoA/RhoC Up-regulation, Leading to Rho-kinase-associated Cytoskeleton Activation and Breast Tumor Cell Invasion *

    doi: 10.1074/jbc.M110.162305

    Figure Lengend Snippet: Analyses of HA/CD44-mediated HOXD10 and RhoGTPase expression in MDA-MB-231 cells. Detection of HA/CD44-induced HOXD10 and RhoGTPase (RhoA/RhoC) expression in MDA-MB-231 cells was performed by solubilizing cells with 1% Nonidet P-40 (Nonidet P-40) buffer

    Article Snippet: These cells were then immediately lysed in Nonidet P-40 buffer (50 m m HEPES (pH 7.5), 150 m m NaCl, 20 m m MgCl2 , 1% Nonidet P-40, 1 m m Na3 VO4 , 1 m m NaF, Complete protease inhibitor mixture (Roche Applied Science), 1 m m PMSF, 1× HaltTM phosphatase inhibitor mixture (Pierce)) at 4 °C and centrifuged to obtain the lysates.

    Techniques: Expressing, Multiple Displacement Amplification

    Nuclease and salt resistance of particles assembled in vitro and of authentic, immature particles. Particles assembled in buffer B ( A ), buffer B plus 5% rabbit reticulocyte lysate ( B ), or buffer B plus 2 μM IP5 ( C ), were treated with RNase A (lanes 2) or NaCl (lanes 3). Gag proteins in particles pelleted after treatment were examined by SDS/PAGE and Coomassie blue staining. We estimate that > 90% of the Gag protein was solubilized in A (lanes 2 and 3), whereas > 90% remained pelletable in B and C (lanes 2 and 3). ( D ) Immature MoMuLV and HIV-1 virions produced in mammalian cells were analyzed separately (lanes 1 and 2, respectively) or were mixed together (lanes 3–9) and treated with RNase A (lanes 6 and 7) or NaCl (lanes 8 and 9). They were also digested with HIV-1 PR to confirm that the lipid envelope was removed by the detergent (lane 3), or sedimented without RNase or NaCl treatment to confirm that the particles are stable in buffer B (lanes 4 and 5). Gag proteins in the samples in D were detected by immunoblotting with antibodies against the CA proteins of both HIV-1 and MoMuLV. We estimate that > 90% of the HIV-1 Gag protein was still pelletable after NaCl or RNase treatment. P, pellet; S, supernatant.

    Journal: Proceedings of the National Academy of Sciences of the United States of America

    Article Title: Modulation of HIV-like particle assembly in vitro by inositol phosphates

    doi: 10.1073/pnas.191224698

    Figure Lengend Snippet: Nuclease and salt resistance of particles assembled in vitro and of authentic, immature particles. Particles assembled in buffer B ( A ), buffer B plus 5% rabbit reticulocyte lysate ( B ), or buffer B plus 2 μM IP5 ( C ), were treated with RNase A (lanes 2) or NaCl (lanes 3). Gag proteins in particles pelleted after treatment were examined by SDS/PAGE and Coomassie blue staining. We estimate that > 90% of the Gag protein was solubilized in A (lanes 2 and 3), whereas > 90% remained pelletable in B and C (lanes 2 and 3). ( D ) Immature MoMuLV and HIV-1 virions produced in mammalian cells were analyzed separately (lanes 1 and 2, respectively) or were mixed together (lanes 3–9) and treated with RNase A (lanes 6 and 7) or NaCl (lanes 8 and 9). They were also digested with HIV-1 PR to confirm that the lipid envelope was removed by the detergent (lane 3), or sedimented without RNase or NaCl treatment to confirm that the particles are stable in buffer B (lanes 4 and 5). Gag proteins in the samples in D were detected by immunoblotting with antibodies against the CA proteins of both HIV-1 and MoMuLV. We estimate that > 90% of the HIV-1 Gag protein was still pelletable after NaCl or RNase treatment. P, pellet; S, supernatant.

    Article Snippet: Particles were assembled in 100 μl of buffer B (buffer A + 1% Nonidet P-40; Roche Molecular Biochemicals).

    Techniques: In Vitro, SDS Page, Staining, Produced

    Automethylation of SUV39H2 is validated in vivo A. Determination of the titer and specificity of the anti-K392 dimethylated SUV39H2 (Sigma-Aldrich) antibody analyzed by enzyme-linked immunosorbent assay (ELISA). A constant amount of K392 methyl peptide or unmethyl peptide has been coated into the wells of the ELISA, and tested with different dilutions of the antibody. B. His-tagged SUV39H2 recombinant proteins were incubated with or without the cofactor SAM at 30°C for 2 hours. Automethylated SUV39H2 protein was blotted with the anti-SUV39H2 K392me2 antibody, and amounts of loading SUV39H2 recombinant proteins were measured by staining with Coomassie Brilliant Blue. C. In vivo methyltransferase experiment was conducted in 293T cells overexpressing FLAG control empty vector (FLAG-Mock), FLAG-tagged SUV39H2 wild-type (FLAG-SUV39H2-WT), FLAG-tagged SUV39H2 K392A mutant (FLAG-SUV39H2-K392A) or FLAG-tagged SUV39H2 K392R mutant (FLAG-SUV39H2-K293R). Cells were lysed with RIPA buffer 48 hours after transfection, and samples were immunoblotted with anti-FLAG and anti-SUV39H2 K392me2 antibodies.

    Journal: Oncotarget

    Article Title: Automethylation of SUV39H2, an oncogenic histone lysine methyltransferase, regulates its binding affinity to substrate proteins

    doi: 10.18632/oncotarget.8072

    Figure Lengend Snippet: Automethylation of SUV39H2 is validated in vivo A. Determination of the titer and specificity of the anti-K392 dimethylated SUV39H2 (Sigma-Aldrich) antibody analyzed by enzyme-linked immunosorbent assay (ELISA). A constant amount of K392 methyl peptide or unmethyl peptide has been coated into the wells of the ELISA, and tested with different dilutions of the antibody. B. His-tagged SUV39H2 recombinant proteins were incubated with or without the cofactor SAM at 30°C for 2 hours. Automethylated SUV39H2 protein was blotted with the anti-SUV39H2 K392me2 antibody, and amounts of loading SUV39H2 recombinant proteins were measured by staining with Coomassie Brilliant Blue. C. In vivo methyltransferase experiment was conducted in 293T cells overexpressing FLAG control empty vector (FLAG-Mock), FLAG-tagged SUV39H2 wild-type (FLAG-SUV39H2-WT), FLAG-tagged SUV39H2 K392A mutant (FLAG-SUV39H2-K392A) or FLAG-tagged SUV39H2 K392R mutant (FLAG-SUV39H2-K293R). Cells were lysed with RIPA buffer 48 hours after transfection, and samples were immunoblotted with anti-FLAG and anti-SUV39H2 K392me2 antibodies.

    Article Snippet: After cell attachment, the cells were transfected with expression vectors using FuGENE™ 6 (Promega, Fitchburg, WI), and after 48 hours of incubation, transfected 293T cells were washed with PBS and lysed by RIPA buffer (50 mM Tris-Cl pH 7.4, 150 mM NaCl, 0.5% sodium deoxycholate, 0.1% SDS, 1% Nonidet-P40, 0.1 mM PMSF) with complete protease inhibitor cocktail (Roche Applied Science, Penzberg, Germany).

    Techniques: In Vivo, Enzyme-linked Immunosorbent Assay, Recombinant, Incubation, Staining, Plasmid Preparation, Mutagenesis, Transfection

    Automethylation of SUV39H2 blocks the protein-substrate interaction A. 293T cells were co-expressed with HA-tagged LSD1 and FLAG-tagged SUV39H2-WT, SUV39H2-K392A or SUV39H2-K392R. After 48 hours of incubation, cells were lysed with RIPA buffer, followed by immunoprecipitation with anti-FLAG M2 affinity gel. Immunoprecipitates were immunoblotted with anti-FLAG and anti-HA antibodies. B. 293T cells were transfected with FLAG-tagged SUV39H2-WT, SUV39H2-K392A or SUV39H2-K392R. Interaction of endogenous histone H3 and exogenous SUV39H2 proteins was examined by western blot analysis.

    Journal: Oncotarget

    Article Title: Automethylation of SUV39H2, an oncogenic histone lysine methyltransferase, regulates its binding affinity to substrate proteins

    doi: 10.18632/oncotarget.8072

    Figure Lengend Snippet: Automethylation of SUV39H2 blocks the protein-substrate interaction A. 293T cells were co-expressed with HA-tagged LSD1 and FLAG-tagged SUV39H2-WT, SUV39H2-K392A or SUV39H2-K392R. After 48 hours of incubation, cells were lysed with RIPA buffer, followed by immunoprecipitation with anti-FLAG M2 affinity gel. Immunoprecipitates were immunoblotted with anti-FLAG and anti-HA antibodies. B. 293T cells were transfected with FLAG-tagged SUV39H2-WT, SUV39H2-K392A or SUV39H2-K392R. Interaction of endogenous histone H3 and exogenous SUV39H2 proteins was examined by western blot analysis.

    Article Snippet: After cell attachment, the cells were transfected with expression vectors using FuGENE™ 6 (Promega, Fitchburg, WI), and after 48 hours of incubation, transfected 293T cells were washed with PBS and lysed by RIPA buffer (50 mM Tris-Cl pH 7.4, 150 mM NaCl, 0.5% sodium deoxycholate, 0.1% SDS, 1% Nonidet-P40, 0.1 mM PMSF) with complete protease inhibitor cocktail (Roche Applied Science, Penzberg, Germany).

    Techniques: Incubation, Immunoprecipitation, Transfection, Western Blot

    TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 immunoprecipitation (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P

    Journal: Oncogenesis

    Article Title: Dysregulation of the MiR-449b target TGFBI alters the TGFβ pathway to induce cisplatin resistance in nasopharyngeal carcinoma

    doi: 10.1038/s41389-018-0050-x

    Figure Lengend Snippet: TGFBI regulates signaling pathways by binding ITGB3 and ITGB5. a ITGB3 immunoprecipitation (IP: αMyc) was performed on HEK293T cells expressing ITGB3 in the absence or the presence of TGFBI (via transfection). Interaction between ITGB3 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. b ITGB5 immunoprecipitation (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC with or without presence of TGFBI (via transfection). Interaction between ITGB5 and TGFBI was detected using anti-TGFBI (αTGFBI) antibody. c Immunoprecipitation of pro-TGFβ1 (IP: αFlag) was performed on HEK293T cells expressing pro-TGFβ1 alone or with ITGB3. Interaction between ITGB3 and pro-TGFβ1 was identified using anti-Myc (αMyc) antibody. d Immunoprecipitation of ITGB5 (IP: αGFP) was performed on HEK293T cells expressing ITGB5ΔC alone or with pro-TGFβ1. Interaction between ITGB5 and pro-TGFβ1 was revealed using anti-Flag (αFlag) antibody. e Co-immunoprecipitations were performed on HEK293T cells expressing ITGB3 alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB3 binding. f Co-immunoprecipitations were performed on HEK293T expressing ITGB5ΔC alone or with pro-TGFβ1 in the absence (TGFβ1-Flag) or presence of TGFBI (TGFβ1-Flag + TGFBI). These data show competition between TGFBI and pro-TGFβ1 for ITGB5 binding. For a–f Western blot of the whole-cell lysates (WCLs) before pull-down is shown as a control for specificity and expression. g Top: relative luciferase activity was assessed after transient transfection of pro-TGFβ1-Flag and TGFBI-Myc, as indicated, and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot of HEK293T cells transfected with pro-TGFβ1-Flag encoding plasmid (1 µg) and TGFBI-Myc encoding plasmid, as indicated. Anti-Myc (αMyc) antibody was used to assess the expression of TGFBI, and anti-Flag (αFlag) antibody was used to assess the expression of pro-TGFβ1 and active TGFβ1 forms. The expression of pro-TGFβ1 indicates similar transfection efficiency across the conditions. Anti-β-actin (αβ-actin) antibody was used as the loading control. h Top: relative luciferase activity was assessed after transient transfection of ITGB3-Myc (1 µg) or ITGB5ΔC-GFP (1 µg) and TGFBI (2 µg), and the co-transfection of pSBE4-luciferase vector (150 ng) and Renilla plasmid (100 ng). Bottom: western blot control of the plasmids expression: anti-TGFBI (αTGFBI) antibody was used to assess the expression of TGFBI, anti-Myc (αMyc), and anti-GFP (αGFP) for ITGB3 and ITGB5, respectively. Anti-β-actin (αβ-actin) antibody was used as the loading control. The data are expressed as the mean ± SEM of at least three independent experiments. * P

    Article Snippet: For both western blot and co-immunoprecipitation, proteins were extracted using immunoprecipitation buffer (50 mM Hepes pH 7.6, 150 mM NaCl, 5 mM EDTA, 1–2% Nonidet P-40) in the presence of protease inhibitor cocktail (Roche, Basel, Switzerland), and then separated using a Bolt 4–20% Gel (Life Technologies, Carlsbad, CA, USA).

    Techniques: Binding Assay, Immunoprecipitation, Expressing, Transfection, Western Blot, Luciferase, Activity Assay, Cotransfection, Plasmid Preparation